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FLP2_CAEEL
ID   FLP2_CAEEL              Reviewed;         106 AA.
AC   G5EFN6; G5EDZ1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=FMRFamide-like neuropeptides 2 {ECO:0000305};
DE   Contains:
DE     RecName: Full=SPREPIRF-amide {ECO:0000305|PubMed:15809090, ECO:0000305|PubMed:24533288};
DE   Contains:
DE     RecName: Full=LRGEPIRF-amide {ECO:0000305|PubMed:15809090, ECO:0000305|PubMed:24533288};
DE   Flags: Precursor;
GN   Name=flp-2 {ECO:0000312|WormBase:W07E11.3a};
GN   Synonyms=flp-2a {ECO:0000312|EMBL:AAC08938.1},
GN   flp-2b {ECO:0000312|EMBL:AAC08939.1};
GN   ORFNames=W07E11.3 {ECO:0000312|WormBase:W07E11.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=15809090; DOI=10.1016/j.bbrc.2005.03.071;
RA   Mertens I., Meeusen T., Janssen T., Nachman R., Schoofs L.;
RT   "Molecular characterization of two G protein-coupled receptor splice
RT   variants as FLP2 receptors in Caenorhabditis elegans.";
RL   Biochem. Biophys. Res. Commun. 330:967-974(2005).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=24533288; DOI=10.1016/j.ijpddr.2012.10.002;
RA   Larsen M.J., Lancheros E.R., Williams T., Lowery D.E., Geary T.G.,
RA   Kubiak T.M.;
RT   "Functional expression and characterization of the C. elegans G-protein-
RT   coupled FLP-2 Receptor (T19F4.1) in mammalian cells and yeast.";
RL   Int. J. Parasitol. Drugs Drug Resist. 3:1-7(2013).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27767096; DOI=10.1038/cr.2016.118;
RA   Shao L.W., Niu R., Liu Y.;
RT   "Neuropeptide signals cell non-autonomous mitochondrial unfolded protein
RT   response.";
RL   Cell Res. 26:1182-1196(2016).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=27585848; DOI=10.1534/genetics.116.192898;
RA   Chen D., Taylor K.P., Hall Q., Kaplan J.M.;
RT   "The Neuropeptides FLP-2 and PDF-1 Act in Concert To Arouse Caenorhabditis
RT   elegans Locomotion.";
RL   Genetics 204:1151-1159(2016).
CC   -!- FUNCTION: FMRFamide-like neuropeptides (PubMed:15809090,
CC       PubMed:24533288). Involved in mediating arousal from the sleep-like
CC       state called lethargus, which occurs during molting between larval and
CC       adult stages, in part by regulating touch sensitivity, and working in
CC       concert with neuropeptide pdf-1 (PubMed:27585848). Involved in neural
CC       modulation of systemic mitochondrial unfolded protein response
CC       (PubMed:27767096). {ECO:0000269|PubMed:15809090,
CC       ECO:0000269|PubMed:24533288, ECO:0000269|PubMed:27585848,
CC       ECO:0000269|PubMed:27767096}.
CC   -!- FUNCTION: [SPREPIRF-amide]: Acts as a ligand to FMRFamide peptide
CC       receptor frpr-18 in vitro. {ECO:0000269|PubMed:15809090,
CC       ECO:0000269|PubMed:24533288}.
CC   -!- FUNCTION: [LRGEPIRF-amide]: Acts as a ligand to FMRFamide peptide
CC       receptor frpr-18 in vitro. {ECO:0000269|PubMed:15809090,
CC       ECO:0000269|PubMed:24533288}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:W07E11.3a};
CC         IsoId=G5EFN6-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:W07E11.3b};
CC         IsoId=G5EFN6-2; Sequence=VSP_061253;
CC   -!- DISRUPTION PHENOTYPE: Knockouts generated by CRISPR-Cas9-mediated gene
CC       editing strongly inhibited the peripheral induction of the
CC       mitochondrial unfolded protein response. {ECO:0000269|PubMed:27767096}.
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DR   EMBL; AF042387; AAC08938.1; -; mRNA.
DR   EMBL; AF042388; AAC08939.1; -; mRNA.
DR   EMBL; BX284606; CAA90031.1; -; Genomic_DNA.
DR   EMBL; BX284606; CAC42354.1; -; Genomic_DNA.
DR   PIR; T26263; T26263.
DR   PIR; T42409; T42409.
DR   RefSeq; NP_001024945.1; NM_001029774.2.
DR   AlphaFoldDB; G5EFN6; -.
DR   SMR; G5EFN6; -.
DR   STRING; 6239.W07E11.3a; -.
DR   PaxDb; G5EFN6; -.
DR   EnsemblMetazoa; W07E11.3a.1; W07E11.3a.1; WBGene00001445. [G5EFN6-1]
DR   EnsemblMetazoa; W07E11.3b.1; W07E11.3b.1; WBGene00001445. [G5EFN6-2]
DR   GeneID; 181222; -.
DR   CTD; 181222; -.
DR   WormBase; W07E11.3a; CE02374; WBGene00001445; flp-2.
DR   WormBase; W07E11.3b; CE28258; WBGene00001445; flp-2.
DR   eggNOG; ENOG502TI3P; Eukaryota.
DR   HOGENOM; CLU_177989_0_0_1; -.
DR   InParanoid; G5EFN6; -.
DR   OMA; VQPKRIL; -.
DR   OrthoDB; 1789029at2759; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001445; Expressed in larva and 3 other tissues.
DR   ExpressionAtlas; G5EFN6; baseline and differential.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR   GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:UniProtKB.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IGI:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR   GO; GO:0030431; P:sleep; IGI:UniProtKB.
PE   3: Inferred from homology;
KW   Alternative splicing; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..106
FT                   /note="FMRFamide-like neuropeptides 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5015091973"
FT   PEPTIDE         75..82
FT                   /note="LRGEPIRF-amide"
FT                   /evidence="ECO:0000269|PubMed:15809090"
FT                   /id="PRO_0000454191"
FT   PEPTIDE         86..93
FT                   /note="SPREPIRF-amide"
FT                   /evidence="ECO:0000269|PubMed:15809090"
FT                   /id="PRO_0000454190"
FT   REGION          82..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         19..49
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_061253"
SQ   SEQUENCE   106 AA;  11897 MW;  C8512718002DE1D7 CRC64;
     MQVSGILSAL FLVLLAVIVS PFQFVQPKRI LPIPTSRDQL LRGQLAYLKG TTVAQPAVND
     NTLGIFEASA MAKRLRGEPI RFGKRSPREP IRFGKRFNPL PDYDFQ
 
 
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